446822-71-5 Usage
Uses
Different sources of media describe the Uses of 446822-71-5 differently. You can refer to the following data:
1. Traceless Staudinger ligation reagent with borane protecting group. The borane group stabilizes the phosphine against oxidation and can be easily removed with mild basic or acidic conditions to yield the active phosphine. After reaction with an azide, the phosphine is eliminated in the presence of water to yield a native amide bond. Used in the synthesis of cyclic peptides.
2. Traceless Staudinger ligation reagent with borane protecting group. The borane group stabilizes the phosphine against oxidation and can be easily removed with mild basic or acidic conditions to yield the active phosphine. After reaction with an azide, the phosphine is eliminated in the presence of water to yield a native amide bond.Used in the synthesis of cyclic peptides.
Check Digit Verification of cas no
The CAS Registry Mumber 446822-71-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 4,4,6,8,2 and 2 respectively; the second part has 2 digits, 7 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 446822-71:
(8*4)+(7*4)+(6*6)+(5*8)+(4*2)+(3*2)+(2*7)+(1*1)=165
165 % 10 = 5
So 446822-71-5 is a valid CAS Registry Number.
446822-71-5Relevant articles and documents
A Versatile Approach for Site-Specific Lysine Acylation in Proteins
Wang, Zhipeng A.,Kurra, Yadagiri,Wang, Xin,Zeng, Yu,Lee, Yan-Jiun,Sharma, Vangmayee,Lin, Hening,Dai, Susie Y.,Liu, Wenshe R.
, p. 1643 - 1647 (2017/02/05)
Using amber suppression in coordination with a mutant pyrrolysyl-tRNA synthetase-tRNAPylpair, azidonorleucine is genetically encoded in E. coli. Its genetic incorporation followed by traceless Staudinger ligation with a phosphinothioester allows the convenient synthesis of a protein with a site-specifically installed lysine acylation. By simply changing the phosphinothioester identity, any lysine acylation type could be introduced. Using this approach, we demonstrated that both lysine acetylation and lysine succinylation can be installed selectively in ubiquitin and synthesized histone H3 with succinylation at its K4 position (H3K4su). Using an H3K4su-H4 tetramer as a substrate, we further confirmed that Sirt5 is an active histone desuccinylase. Lysine succinylation is a recently identified post-translational modification. The reported technique makes it possible to explicate regulatory functions of this modification in proteins.
